ANALYSIS OF THE STRUCTURAL BASES OF THERMOSTABILITY OF SECRETED BACILLARY METALLOPROTEINASES WITH MODEL CHIMERIC ENZYMES

被引：0

作者：

CHUMAKOV, VN ^{[1
]}

AZIMOVA, MI ^{[1
]}

ZAITSEV, DA ^{[1
]}

GABRIELYAN, AE ^{[1
]}

KOSTROV, SV ^{[1
]}

机构：

[1] VA ENGELHARDT MOLEC BIOL INST,MOSCOW 117984,RUSSIA

来源：

MOLECULAR BIOLOGY | 1995年 / 29卷 / 05期

关键词：

BACILLI; PROTEINASES; RECOMBINATION; STRUCTURE; THERMOSTABILITY;

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Six chimeric bacillary metalloproteinases were purified from culture media of Bacillus subtilis expressing hybrid genes earlier created by homologous recombination. The heat stability and temperature optima were examined for natural secreted metalloproteinases of Bac. amyloliquefaciens and Bac. brevis and their structural hybrids. These experimental data together with the results of computer analysis made it possible to locate additional structural regions essential for the thermal stability of the enzyme molecule as a whole.

引用

页码：578 / 583

页数：6